Structure of eIF3b RNA recognition motif and its interaction with eIF3j: structural insights into the recruitment of eIF3b to the 40 S ribosomal subunit
| dc.contributor.author | ElAntak, L. | en |
| dc.contributor.author | Tzakos, A. G. | en |
| dc.contributor.author | Locker, N. | en |
| dc.contributor.author | Lukavsky, P. J. | en |
| dc.date.accessioned | 2015-11-24T16:48:21Z | |
| dc.date.available | 2015-11-24T16:48:21Z | |
| dc.identifier.issn | 0021-9258 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/9307 | |
| dc.rights | Default Licence | - |
| dc.subject | Amino Acid Motifs | en |
| dc.subject | Amino Acid Sequence | en |
| dc.subject | Eukaryotic Initiation Factor-3/*chemistry | en |
| dc.subject | Humans | en |
| dc.subject | Magnetic Resonance Spectroscopy | en |
| dc.subject | Molecular Conformation | en |
| dc.subject | Molecular Sequence Data | en |
| dc.subject | Peptide Initiation Factors/chemistry | en |
| dc.subject | Protein Binding | en |
| dc.subject | Protein Biosynthesis | en |
| dc.subject | Protein Structure, Secondary | en |
| dc.subject | Protein Structure, Tertiary | en |
| dc.subject | Ribosomes/chemistry | en |
| dc.subject | Sequence Homology, Amino Acid | en |
| dc.title | Structure of eIF3b RNA recognition motif and its interaction with eIF3j: structural insights into the recruitment of eIF3b to the 40 S ribosomal subunit | en |
| heal.abstract | Mammalian eIF3 is a 700-kDa multiprotein complex essential for initiation of protein synthesis in eukaryotic cells. It consists of 13 subunits (eIF3a to -m), among which eIF3b serves as a major scaffolding protein. Here we report the solution structure of the N-terminal RNA recognition motif of human eIF3b (eIF3b-RRM) determined by NMR spectroscopy. The structure reveals a noncanonical RRM with a negatively charged surface in the beta-sheet area contradictory with potential RNA binding activity. Instead, eIF3j, which is required for stable 40 S ribosome binding of the eIF3 complex, specifically binds to the rear alpha-helices of the eIF3b-RRM, opposite to its beta-sheet surface. Moreover, we identify that an N-terminal 69-amino acid peptide of eIF3j is sufficient for binding to eIF3b-RRM and that this interaction is essential for eIF3b-RRM recruitment to the 40 S ribosomal subunit. Our results provide the first structure of an important subdomain of a core eIF3 subunit and detailed insights into protein-protein interactions between two eIF3 subunits required for stable eIF3 recruitment to the 40 S subunit. | en |
| heal.access | campus | - |
| heal.fullTextAvailability | TRUE | - |
| heal.identifier.primary | 10.1074/jbc.M610860200 | - |
| heal.identifier.secondary | http://www.ncbi.nlm.nih.gov/pubmed/17190833 | - |
| heal.identifier.secondary | http://www.jbc.org/content/282/11/8165.full.pdf | - |
| heal.journalName | J Biol Chem | en |
| heal.journalType | peer reviewed | - |
| heal.language | en | - |
| heal.publicationDate | 2007 | - |
| heal.publisher | The American Society for Biochemistry and Molecular Biology, Inc. | en |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας | el |
| heal.type | journalArticle | - |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.type.en | Journal article | en |
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